3jqm

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(New page: '''Unreleased structure''' The entry 3jqm is ON HOLD until Paper Publication Authors: Kanaujia, S.P., Jeyakanthan, J., Nakagawa, N., Sekar, K., Shinkai, A., Kuramitsu, S., Yokoyama, S.,...)
Current revision (16:04, 1 November 2023) (edit) (undo)
 
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'''Unreleased structure'''
 
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The entry 3jqm is ON HOLD until Paper Publication
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==Binding of 5'-GTP to molybdenum cofactor biosynthesis protein MoaC from Thermus theromophilus HB8==
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<StructureSection load='3jqm' size='340' side='right'caption='[[3jqm]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[3jqm]] is a 9 chain structure with sequence from [https://en.wikipedia.org/wiki/Thermus_thermophilus_HB8 Thermus thermophilus HB8]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3JQM OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3JQM FirstGlance]. <br>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.5&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=FLC:CITRATE+ANION'>FLC</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=GTP:GUANOSINE-5-TRIPHOSPHATE'>GTP</scene>, <scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</scene></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3jqm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3jqm OCA], [https://pdbe.org/3jqm PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3jqm RCSB], [https://www.ebi.ac.uk/pdbsum/3jqm PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3jqm ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/Q5SHE1_THET8 Q5SHE1_THET8] Together with MoaA, is involved in the conversion of 5'-GTP to cyclic pyranopterin monophosphate (cPMP or molybdopterin precursor Z) (By similarity).[HAMAP-Rule:MF_01224][SAAS:SAAS002820_004_012265]
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/jq/3jqm_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=3jqm ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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The first step in the molybdenum cofactor (Moco) biosynthesis pathway involves the conversion of guanosine triphosphate (GTP) to precursor Z by two proteins (MoaA and MoaC). MoaA belongs to the S-adenosylmethionine-dependent radical enzyme superfamily and is believed to generate protein and/or substrate radicals by reductive cleavage of S-adenosylmethionine using an Fe-S cluster. MoaC has been suggested to catalyze the release of pyrophosphate and the formation of the cyclic phosphate of precursor Z. However, structural evidence showing the binding of a substrate-like molecule to MoaC is not available. Here, apo and GTP-bound crystal structures of MoaC from Thermus thermophilus HB8 are reported. Furthermore, isothermal titration calorimetry experiments have been carried out in order to obtain thermodynamic parameters for the protein-ligand interactions. In addition, molecular-dynamics (MD) simulations have been carried out on the protein-ligand complex of known structure and on models of relevant complexes for which X-ray structures are not available. The biophysical, structural and MD results reveal the residues that are involved in substrate binding and help in speculating upon a possible mechanism.
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Authors: Kanaujia, S.P., Jeyakanthan, J., Nakagawa, N., Sekar, K., Shinkai, A., Kuramitsu, S., Yokoyama, S., Riken Structural Genomics/Proteomics Initiative (Rsgi)
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Structures of apo and GTP-bound molybdenum cofactor biosynthesis protein MoaC from Thermus thermophilus HB8.,Kanaujia SP, Jeyakanthan J, Nakagawa N, Balasubramaniam S, Shinkai A, Kuramitsu S, Yokoyama S, Sekar K Acta Crystallogr D Biol Crystallogr. 2010 Jul;66(Pt 7):821-33. Epub 2010 Jun 19. PMID:20606263<ref>PMID:20606263</ref>
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Description: BINDING OF 5'-GTP TO MOLYBDENUM COFACTOR BIOSYNTHESIS PROTEIN MoaC FROM THERMUS THEROMOPHILUS HB8
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Sep 16 08:45:27 2009''
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<div class="pdbe-citations 3jqm" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Large Structures]]
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[[Category: Thermus thermophilus HB8]]
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[[Category: Jeyakanthan J]]
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[[Category: Kanaujia SP]]
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[[Category: Kuramitsu S]]
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[[Category: Nakagawa N]]
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[[Category: Sekar K]]
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[[Category: Shinkai A]]
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[[Category: Yokoyama S]]

Current revision

Binding of 5'-GTP to molybdenum cofactor biosynthesis protein MoaC from Thermus theromophilus HB8

PDB ID 3jqm

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